Amyloid-like protein inclusions in tobacco transgenic plants.
The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the struc...
Main Authors: | , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2010-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC2964307?pdf=render |
_version_ | 1818030572446941184 |
---|---|
author | Anna Villar-Piqué Raimon Sabaté Oriol Lopera Jordi Gibert Josep Maria Torne Mireya Santos Salvador Ventura |
author_facet | Anna Villar-Piqué Raimon Sabaté Oriol Lopera Jordi Gibert Josep Maria Torne Mireya Santos Salvador Ventura |
author_sort | Anna Villar-Piqué |
collection | DOAJ |
description | The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the structure of the inclusions formed by maize transglutaminase (TGZ) in the chloroplasts of tobacco transplastomic plants and demonstrate that they have an amyloid-like nature. Together with the evidence of amyloid structures in bacteria and fungi our data argue that amyloid formation is likely a ubiquitous process occurring across the different kingdoms of life. The discovery of amyloid conformations inside inclusions of genetically modified plants might have implications regarding their use for human applications. |
first_indexed | 2024-12-10T05:37:43Z |
format | Article |
id | doaj.art-40033e8d10864b68b392850371bb84c6 |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-12-10T05:37:43Z |
publishDate | 2010-01-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS ONE |
spelling | doaj.art-40033e8d10864b68b392850371bb84c62022-12-22T02:00:22ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-01-01510e1362510.1371/journal.pone.0013625Amyloid-like protein inclusions in tobacco transgenic plants.Anna Villar-PiquéRaimon SabatéOriol LoperaJordi GibertJosep Maria TorneMireya SantosSalvador VenturaThe formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the structure of the inclusions formed by maize transglutaminase (TGZ) in the chloroplasts of tobacco transplastomic plants and demonstrate that they have an amyloid-like nature. Together with the evidence of amyloid structures in bacteria and fungi our data argue that amyloid formation is likely a ubiquitous process occurring across the different kingdoms of life. The discovery of amyloid conformations inside inclusions of genetically modified plants might have implications regarding their use for human applications.http://europepmc.org/articles/PMC2964307?pdf=render |
spellingShingle | Anna Villar-Piqué Raimon Sabaté Oriol Lopera Jordi Gibert Josep Maria Torne Mireya Santos Salvador Ventura Amyloid-like protein inclusions in tobacco transgenic plants. PLoS ONE |
title | Amyloid-like protein inclusions in tobacco transgenic plants. |
title_full | Amyloid-like protein inclusions in tobacco transgenic plants. |
title_fullStr | Amyloid-like protein inclusions in tobacco transgenic plants. |
title_full_unstemmed | Amyloid-like protein inclusions in tobacco transgenic plants. |
title_short | Amyloid-like protein inclusions in tobacco transgenic plants. |
title_sort | amyloid like protein inclusions in tobacco transgenic plants |
url | http://europepmc.org/articles/PMC2964307?pdf=render |
work_keys_str_mv | AT annavillarpique amyloidlikeproteininclusionsintobaccotransgenicplants AT raimonsabate amyloidlikeproteininclusionsintobaccotransgenicplants AT oriollopera amyloidlikeproteininclusionsintobaccotransgenicplants AT jordigibert amyloidlikeproteininclusionsintobaccotransgenicplants AT josepmariatorne amyloidlikeproteininclusionsintobaccotransgenicplants AT mireyasantos amyloidlikeproteininclusionsintobaccotransgenicplants AT salvadorventura amyloidlikeproteininclusionsintobaccotransgenicplants |